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The immunoglobulin fold. Structural classification, sequence patterns and common core

P Bork1, L Holm, C Sander

  • 1EMBL, Heidelberg, Germany.

Journal of Molecular Biology
|September 30, 1994
PubMed
Summary
This summary is machine-generated.

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This study reveals a common four-beta-strand core in immunoglobulin domains, despite diverse functions. Variations in surrounding strands define four subtypes, showing flexibility rather than a single folding pathway.

Area of Science:

  • Structural biology
  • Protein domains
  • Bioinformatics

Background:

  • Immunoglobulin (Ig) domains possess a conserved modular architecture.
  • This characteristic beta-sheet fold appears in proteins with diverse biological functions.

Purpose of the Study:

  • To systematically compare Ig domain structures with low sequence identity.
  • To identify conserved structural elements and topological variations.

Main Methods:

  • Automatic structural alignment of 23 Ig domain structures.
  • Analysis of beta-sheet and loop topology.
  • Identification of sequence consensus patterns.

Main Results:

  • A common structural core of four beta-strands (b, c, e, f) was identified.

Related Experiment Videos

  • Four distinct topological subtypes were defined based on variations in edge strands.
  • The length of the c-e sequence segment correlates with topological differences.

    • Conclusions:

    • Ig domain structure exhibits flexibility outside the core, challenging a universal folding pathway.
    • Disulfide bridges are not universally conserved in number or location within subclasses.